ANXA8L1 Human

Annexin A8 Like-1 Human Recombinant
Cat. No.
BT21153
Source
E.coli.
Synonyms
Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

ANXA8L1 Human Recombinant produced in E. coli is a single polypeptide chain containing 351 amino acids (1-327) and having a molecular mass of 39.4 kDa.
ANXA8L1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Annexin A8-like 2 (ANXA8L2), a member of the annexin family, is a calcium-dependent phospholipid binding protein. Annexins regulate diverse cellular processes, including ion flux, endocytosis, exocytosis, and cellular adhesion. ANXA8L2 exhibits multiple functions, acting as a voltage-sensitive calcium channel, displaying ion selectivity, and mediating membrane fusion. Overexpression of ANXA8L2 is implicated in acute myelocytic leukemia. Additionally, ANXA8L2 may function as an anticoagulant by indirectly inhibiting the thromboplastin-specific complex.
Description
Recombinant human ANXA8L1, expressed in E. coli, is a single polypeptide chain with a molecular weight of 39.4 kDa. It consists of 351 amino acids, spanning positions 1 to 327. The protein has a 24 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The ANXA8L1 solution is provided at a concentration of 1 mg/ml and is formulated in 20 mM Tris-HCl buffer (pH 8.0), 0.1 M NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the ANXA8L1 protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAWWKA WIEQEGVTVK SSSHFNPDPD AETLYKAMKG IGTNEQAIID VLTKRSNTQR QQIAKSFKAQ FGKDLTETLK SELSGKFERL IVALMYPPYR YEAKELHDAM KGLGTKEGVI IEILASRTKN QLREIMKAYE EDYGSSLEED IQADTSGYLE RILVCLLQGS RDDVSSFVDP ALALQDAQDL YAAGENIRGT DEMKFITILC TRSATHLLRV FEEYEKIANK SIEDSIKSET HGSLEEAMLT VVKCTQNLHS YFAERLYYAM KGAGTRDGTL IRNIVSRSEI DLNLIKCHFK KMYGKTLSSM IMEDTSGDYK NALLSLVGSD P

Product Science Overview

Gene and Protein Structure

The ANXA8L1 gene is located on the long arm of chromosome 10. It encodes a protein that is structurally similar to other annexins, characterized by the presence of four annexin repeats. These repeats are responsible for the calcium-dependent binding to phospholipids .

Biological Functions

Annexin A8 Like-1 is implicated in several biological functions:

  • Anticoagulant Activity: The protein may function as an anticoagulant by indirectly inhibiting the thromboplastin-specific complex .
  • Cellular Processes: It plays a role in ion flux, endocytosis, exocytosis, and cellular adhesion .
Clinical Significance

Overexpression of ANXA8L1 has been associated with acute myelocytic leukemia, suggesting its potential role in the pathogenesis of this disease . Additionally, Annexin A8 has been identified as a potential prognostic biomarker and therapeutic target for ovarian cancer. High expression levels of ANXA8 are correlated with poor prognosis in ovarian cancer patients .

Research and Applications

Recombinant human Annexin A8 Like-1 is used in various research applications to study its role in cellular processes and disease mechanisms. It is also utilized in the development of potential therapeutic strategies targeting annexin-related pathways .

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